ID   A0A428NZB5_9HYPO        Unreviewed;       447 AA.
AC   A0A428NZB5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Saccharopine dehydrogenase [NADP(+), L-glutamate-forming] {ECO:0000313|EMBL:RSL46057.1};
GN   ORFNames=CEP54_014008 {ECO:0000313|EMBL:RSL46057.1};
OS   Fusarium duplospermum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=1325734 {ECO:0000313|EMBL:RSL46057.1, ECO:0000313|Proteomes:UP000288168};
RN   [1] {ECO:0000313|EMBL:RSL46057.1, ECO:0000313|Proteomes:UP000288168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62584 {ECO:0000313|EMBL:RSL46057.1,
RC   ECO:0000313|Proteomes:UP000288168};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RSL46057.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NKCI01000247; RSL46057.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428NZB5; -.
DR   STRING; 1325734.A0A428NZB5; -.
DR   Proteomes; UP000288168; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009085; P:lysine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1870.10; Domain 3, Saccharopine reductase; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032095; Sacchrp_dh-like_C.
DR   InterPro; IPR005097; Sacchrp_dh_NADP.
DR   PANTHER; PTHR11133:SF25; ALPHA-AMINOADIPIC SEMIALDEHYDE SYNTHASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11133; SACCHAROPINE DEHYDROGENASE; 1.
DR   Pfam; PF16653; Sacchrp_dh_C; 1.
DR   Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288168}.
FT   DOMAIN          6..120
FT                   /note="Saccharopine dehydrogenase NADP binding"
FT                   /evidence="ECO:0000259|Pfam:PF03435"
FT   DOMAIN          124..439
FT                   /note="Saccharopine dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16653"
SQ   SEQUENCE   447 AA;  48821 MW;  4461E88D1E96D152 CRC64;
     MAQQSVLMLG AGFVTRPTLD VLTQSGIPVT VACRTLETAK KLSEGVNLAT PISLDVSDEK
     ALDAEVAKHD LVISLIPYTF HALVIKSAIR NKKNVVTTSY VSPAMMELDE EAKAAGITVM
     NEIGVDPGVD HLYAVKTIEE VHAGGGKILS FLSYCGGLPA PEVSGNPLGY KFSWSSRGVL
     LALRNAARYY QDGKIADVAS KDLMGTAKPY FIYPGFAFVA YPNRDSTPYK ERYNIPEAET
     IIRGTLRYQG FPQFIRVLVQ IGFLDDTAQE ALSQPIAWNE ATKIIVGAKS SSAADLEEAI
     VSKATFDSPE DQKRILSGLR WIGLFSDEKI TPRGNPLDTL CATLEKKMQF EEGERDLVML
     QHKFEIEHKD GSRETRTSTL VEYGDPKGYS AMARLVGVPC AVAVKQVLNG TLSEKGILAP
     MNGKINNPIL KELKEEYGIF CVEETVS
//